GEMI6_MOUSE
ID GEMI6_MOUSE Reviewed; 166 AA.
AC Q9CX53; Q3TIW7; Q9CQI0; Q9CXC5;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2003, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Gem-associated protein 6;
DE Short=Gemin-6;
GN Name=Gemin6;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=BALB/cJ, and C57BL/6J; TISSUE=Embryo, Liver, Lung, and Mesonephros;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: The SMN complex catalyzes the assembly of small nuclear
CC ribonucleoproteins (snRNPs), the building blocks of the spliceosome,
CC and thereby plays an important role in the splicing of cellular pre-
CC mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins
CC SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in
CC a heptameric protein ring on the Sm site of the small nuclear RNA to
CC form the core snRNP (Sm core). In the cytosol, the Sm proteins SNRPD1,
CC SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm
CC complex by the chaperone CLNS1A that controls the assembly of the core
CC snRNP. To assemble core snRNPs, the SMN complex accepts the trapped 5Sm
CC proteins from CLNS1A forming an intermediate. Binding of snRNA inside
CC 5Sm triggers eviction of the SMN complex, thereby allowing binding of
CC SNRPD3 and SNRPB to complete assembly of the core snRNP (By
CC similarity). {ECO:0000250|UniProtKB:Q8WXD5}.
CC -!- SUBUNIT: Part of the core SMN complex that contains SMN1, GEMIN2/SIP1,
CC DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8 and STRAP/UNRIP.
CC Part of the SMN-Sm complex that contains SMN1, GEMIN2/SIP1,
CC DDX20/GEMIN3, GEMIN4, GEMIN5, GEMIN6, GEMIN7, GEMIN8, STRAP/UNRIP and
CC the Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG.
CC Interacts with GEMIN7; the interaction is direct. Interacts with
CC GEMIN8; the interaction is direct. Interacts with SNRPB, SNRPD2, SNRPD3
CC and SNRPE; the interaction is direct. {ECO:0000250|UniProtKB:Q8WXD5}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000250|UniProtKB:Q8WXD5}. Nucleus, gem
CC {ECO:0000250|UniProtKB:Q8WXD5}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q8WXD5}. Note=Found both in the nucleoplasm and
CC in nuclear bodies called gems (Gemini of Cajal bodies) that are often
CC in proximity to Cajal (coiled) bodies. Also found in the cytoplasm (By
CC similarity). {ECO:0000250}.
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DR EMBL; AK011454; BAB27627.1; -; mRNA.
DR EMBL; AK013396; BAB28830.1; -; mRNA.
DR EMBL; AK018385; BAB31187.1; -; mRNA.
DR EMBL; AK020147; BAB32011.1; -; mRNA.
DR EMBL; AK157745; BAE34178.1; -; mRNA.
DR EMBL; AK167680; BAE39729.1; -; mRNA.
DR EMBL; AK167920; BAE39927.1; -; mRNA.
DR EMBL; BC025157; AAH25157.1; -; mRNA.
DR CCDS; CCDS28989.1; -.
DR RefSeq; NP_080329.1; NM_026053.3.
DR RefSeq; XP_011244883.1; XM_011246581.2.
DR RefSeq; XP_011244884.1; XM_011246582.1.
DR AlphaFoldDB; Q9CX53; -.
DR SMR; Q9CX53; -.
DR IntAct; Q9CX53; 1.
DR MINT; Q9CX53; -.
DR STRING; 10090.ENSMUSP00000063554; -.
DR iPTMnet; Q9CX53; -.
DR PhosphoSitePlus; Q9CX53; -.
DR EPD; Q9CX53; -.
DR MaxQB; Q9CX53; -.
DR PaxDb; Q9CX53; -.
DR PeptideAtlas; Q9CX53; -.
DR PRIDE; Q9CX53; -.
DR ProteomicsDB; 271209; -.
DR Antibodypedia; 29530; 181 antibodies from 26 providers.
DR DNASU; 67242; -.
DR Ensembl; ENSMUST00000069486; ENSMUSP00000063554; ENSMUSG00000055760.
DR GeneID; 67242; -.
DR KEGG; mmu:67242; -.
DR UCSC; uc008dqv.1; mouse.
DR CTD; 79833; -.
DR MGI; MGI:1914492; Gemin6.
DR VEuPathDB; HostDB:ENSMUSG00000055760; -.
DR eggNOG; ENOG502RZTW; Eukaryota.
DR GeneTree; ENSGT00390000006712; -.
DR HOGENOM; CLU_127294_0_0_1; -.
DR InParanoid; Q9CX53; -.
DR OMA; KSPLEWE; -.
DR PhylomeDB; Q9CX53; -.
DR TreeFam; TF314693; -.
DR Reactome; R-MMU-191859; snRNP Assembly.
DR BioGRID-ORCS; 67242; 26 hits in 75 CRISPR screens.
DR ChiTaRS; Gemin6; mouse.
DR PRO; PR:Q9CX53; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q9CX53; protein.
DR Bgee; ENSMUSG00000055760; Expressed in epiblast (generic) and 65 other tissues.
DR Genevisible; Q9CX53; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0097504; C:Gemini of coiled bodies; ISS:UniProtKB.
DR GO; GO:0016604; C:nuclear body; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0032797; C:SMN complex; ISS:UniProtKB.
DR GO; GO:0034719; C:SMN-Sm protein complex; ISS:UniProtKB.
DR GO; GO:0000245; P:spliceosomal complex assembly; IEA:InterPro.
DR GO; GO:0000387; P:spliceosomal snRNP assembly; ISS:UniProtKB.
DR InterPro; IPR009422; Gemin6.
DR PANTHER; PTHR14710; PTHR14710; 1.
DR Pfam; PF06372; Gemin6; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..166
FT /note="Gem-associated protein 6"
FT /id="PRO_0000087461"
FT MOD_RES 94
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WXD5"
FT MOD_RES 165
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8WXD5"
FT CONFLICT 52
FT /note="G -> S (in Ref. 1; BAB31187)"
FT /evidence="ECO:0000305"
FT CONFLICT 157
FT /note="L -> F (in Ref. 1; BAB32011)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 166 AA; 18750 MW; 8A6C06DF6E8E9194 CRC64;
MSEWMKKSPL EWEDYVYKEV RVIACEKEYK GWLLTTDPVS ANIVLVNFLE DGRLSVTGIM
GHSVQTVETI SEGDHRVREK LMHVFASGDC KGYSPEDLEE KRTSLKKWLE KNHIPVTEQG
DAQRTLCVAG VLTIDPPYAP ENCSSSNEII LSRIQDLIQG HLSASQ
